Viral glycoproteins mediate the initial interaction between the virus and the target cell and the host immune response to the virus. The goal of this project is to study Herpes Simplex Virus (HSV) glycoprotein structure, function and expression on HSV infected and transformed cells. The 5 major glycoproteins of HSV, A,B,C,D, and E, will be purified from virions and infected cells by protease or non-ionic detergent solubilization, followed by lectin affinity, ion exchange and molecular sieve chromatography. The glycoproteins will be identified by their chracteristic mobility on SDS gels. Monospecific and monoclonal antibodies will be prepared against each of the glycoproteins to facilitate the identification, localization and purification of the glycoproteins. To study the interaction of HSV with target cells, the purified glycoproteins will be used in direct binding studies and the antisera used for neutralization or blocking of the interaction of radiolabelled glycoproteins and virus with cells. The monoclonal antibodies will be used to localize viral glycoproteins in infected cells, transformed cells and extracellular fluids using immunofluorescence, immunoelectromicroscopy and EIA techniques. Monoclonal antibodies capable of distinguishing HSV type specific determinants will be applied towards clinical diagnostic assays.